Our research activities fall within 3 main areas, which all relate to the study of the kinetics and thermodynamics of protein conformational changes, namely membrane protein folding, protein-detergent interactions and protein fibrillation. These areas are linked by a keen interest in understanding the mechanistic and thermodynamic behaviour of proteins in different circumstances by quantifying the strength of internal side-chain interactions as well as contacts with solvent molecules, whether it be detergents, denaturants, stabilizing salts and osmolytes or lipids. Ultimately we hope this will lead to a greater manipulative ability vis-a-vis processes of both basic, pharmaceutical and industrial relevance. The general approach is to use available spectroscopic techniques (fluorescence, CD, stopped-flow, FTIR, NMR and dynamic and static light scattering) to generate data which can be analyzed in a quantitative manner to develop models and mechanisms for conformational changes at the molecular level.
2020.02.07 | iNano
Controlling protein structure is crucial in the production of detergents and cosmetics. Up to now we have not had a clear understanding of how soap molecules and proteins work together to change protein structure. Now AU researchers have succeeded in creating a detailed picture of both unfolding and refolding of a protein by soap molecules on the…
2020.02.06 | iNano
There are magnets in virtually all modern electrical equipment. However, the current versions are often based on metals with heavy impacts on the environment. Associate Professor Mogens Christensen is researching a new and cleaner magnet technology; research which also opens up for new opportunities to exploit and store electricity.
2020.01.20 | iNano
13 iNANO associated researchers have been granted DKK 8 million from the Carlsberg Foundation for research infrastructure
